Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Studies on analogs of a peptide derived from alpha-fetoprotein having antigrowth properties
Autore:
Eisele, LE; Mesfin, FB; Bennett, JA; Andersen, TT; Jacobson, HI; Vakharia, DD; MacColl, R; Mizejewski, GJ;
Indirizzi:
New York State Dept Hlth, Wadsworth Ctr Labs & Res, Albany, NY 12201 USA New York State Dept Hlth Albany NY USA 12201 & Res, Albany, NY 12201 USA Albany Med Ctr, Albany, NY USA Albany Med Ctr Albany NY USAAlbany Med Ctr, Albany, NY USA
Titolo Testata:
JOURNAL OF PEPTIDE RESEARCH
fascicolo: 6, volume: 57, anno: 2001,
pagine: 539 - 546
SICI:
1397-002X(200106)57:6<539:SOAOAP>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN SECONDARY STRUCTURE; BREAST-CANCER RISK; FETOMATERNAL INTERFACE; THERMODYNAMIC SCALE; CIRCULAR-DICHROISM; MULTIPLE BIRTHS; MATERNAL SERUM; AMINO-ACIDS; FATTY-ACID; ESTRADIOL;
Keywords:
antigrowth peptides; breast cancer treatments; peptide conformation; peptide oligomers; transformed alpha-fetoprotein; trifluoroethanol;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: MacColl, R New York State Dept Hlth, Wadsworth Ctr Labs & Res, POB 509, Albany, NY 12201 USA New York State Dept Hlth POB 509 Albany NY USA 12201 12201 USA
Citazione:
L.E. Eisele et al., "Studies on analogs of a peptide derived from alpha-fetoprotein having antigrowth properties", J PEPT RES, 57(6), 2001, pp. 539-546

Abstract

A 34-amino acid portion of the third domain of alphafetoprotein possesses antigrowth and anticancer activities. Three analogs of this sequence were chemically synthesized, in which the two cysteines of the original sequence were replaced by alanines, glycines or serines. The original cysteine and alanine peptides formed trimers at 0.20 g/L in pH 7.4 phosphate buffer, and the glycine and serine peptides formed dimers. Trimer preparations were more potent in inhibiting estrogen-induced growth in the mouse uterine assays than the two dimeric oligomers. Of salient importance is that the alanine peptide retained its trimeric form in solution much longer than the cysteinepeptide. Antigrowth assays were performed starting with stock solutions ata peptide concentration of 0.20 g/L, because at very high peptide concentration (8.0 g/L) the peptides aggregated extensively. All the peptides, although differing in biological activity, had almost identical secondary structures. Unlike alpha-fetoprotein, the three peptides have low amounts of alpha -helix. Trifluoroethanol has the ability to convert peptides into a helical conformation when they have a propensity for that structure. At trifluoroethanol concentrations of 20% and higher, the alanine and glycine peptides were changed into highly helical structures.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/10/20 alle ore 22:42:46